ID   RUTA_ECOKI              Reviewed;         393 AA.
AC   D5CZH2;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Pyrimidine monooxygenase RutA {ECO:0000255|HAMAP-Rule:MF_01699};
DE            EC=1.14.99.46 {ECO:0000255|HAMAP-Rule:MF_01699};
GN   Name=rutA {ECO:0000255|HAMAP-Rule:MF_01699}; OrderedLocusNames=ECOK1_1064;
OS   Escherichia coli O18:K1:H7 (strain IHE3034 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=714962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHE3034 / ExPEC;
RX   PubMed=20439758; DOI=10.1073/pnas.0915077107;
RA   Moriel D.G., Bertoldi I., Spagnuolo A., Marchi S., Rosini R., Nesta B.,
RA   Pastorello I., Corea V.A., Torricelli G., Cartocci E., Savino S.,
RA   Scarselli M., Dobrindt U., Hacker J., Tettelin H., Tallon L.J.,
RA   Sullivan S., Wieler L.H., Ewers C., Pickard D., Dougan G., Fontana M.R.,
RA   Rappuoli R., Pizza M., Serino L.;
RT   "Identification of protective and broadly conserved vaccine antigens from
RT   the genome of extraintestinal pathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:9072-9077(2010).
CC   -!- FUNCTION: Catalyzes the pyrimidine ring opening between N-3 and C-4 by
CC       an unusual flavin hydroperoxide-catalyzed mechanism, adding oxygen
CC       atoms in the process to yield ureidoacrylate peracid, that immediately
CC       reacts with FMN forming ureidoacrylate and FMN-N(5)-oxide. The FMN-
CC       N(5)-oxide reacts spontaneously with NADH to produce FMN. Requires the
CC       flavin reductase RutF to regenerate FMN in vivo. {ECO:0000255|HAMAP-
CC       Rule:MF_01699}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMNH2 + NADH + O2 + uracil = (Z)-3-ureidoacrylate + FMN + H(+)
CC         + H2O + NAD(+); Xref=Rhea:RHEA:31587, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17568,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57618, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:59891; EC=1.14.99.46;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01699};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FMNH2 + NADH + O2 + thymine = (Z)-2-methylureidoacrylate + FMN
CC         + H(+) + H2O + NAD(+); Xref=Rhea:RHEA:31599, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17821,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57618, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:143783; EC=1.14.99.46;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01699};
CC   -!- INDUCTION: Up-regulated by the nitrogen regulatory protein C (NtrC also
CC       called GlnG) and repressed by RutR. {ECO:0000255|HAMAP-Rule:MF_01699}.
CC   -!- SIMILARITY: Belongs to the NtaA/SnaA/DszA monooxygenase family. RutA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01699}.
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DR   EMBL; CP001969; ADE91825.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5CZH2; -.
DR   SMR; D5CZH2; -.
DR   KEGG; eih:ECOK1_1064; -.
DR   PATRIC; fig|714962.3.peg.1078; -.
DR   HOGENOM; CLU_027853_1_1_6; -.
DR   OMA; ADYNFCF; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0052614; F:uracil oxygenase activity; IEA:RHEA.
DR   GO; GO:0019740; P:nitrogen utilization; IEA:UniProtKB-UniRule.
DR   GO; GO:0006212; P:uracil catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.30; -; 1.
DR   HAMAP; MF_01699; RutA; 1.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   InterPro; IPR019914; Pyrimidine_monooxygenase_RutA.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   SUPFAM; SSF51679; SSF51679; 1.
DR   TIGRFAMs; TIGR03612; RutA; 1.
PE   3: Inferred from homology;
KW   Flavoprotein; FMN; Monooxygenase; NADP; Oxidoreductase.
FT   CHAIN           1..393
FT                   /note="Pyrimidine monooxygenase RutA"
FT                   /id="PRO_0000402612"
FT   BINDING         79..80
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT   BINDING         145
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT   BINDING         154
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT   BINDING         170..171
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
FT   BINDING         220
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01699"
SQ   SEQUENCE   393 AA;  43481 MW;  A6241D961420BFAC CRC64;
     MQTSHYAAEK DMQDAAPRLT FTLRDEERLM MKIGVFVPIG NNGWLISTHA PQYMPTFELN
     KAIVQKAEHY HFDFALSMIK LRGFGGKTEF WDHNLESFTL MAGLAAVTSR IQIYATAATL
     TLPPAIVARM AATIDSISGG RFGVNLVTGW QKPEYEQMGI WPGDDYFSRR YDYLTEYVQV
     LRDLWGSGKS DFKGDFFTMD DCRVSPQPSV PMKVICAGQS DAGMAFSARY ADFNFCFGKG
     VNTPTAFAPT AARMKQAAEQ TGRDVGSYVL FMVIADETDD AARAKWEHYK AGADEEALSW
     LTEQSQKDTR SGTDTNVRQM ADPTSAVNIN MGTLVGSYAS VARMLDEVAS VPGAEGVLLT
     FDDFLSGIEN FGERIQPLMQ CRAHLPALTQ EVA